Open AccessAnalysis of the role of pglI in pilin glycosylation of Neisseria meningitidis
Author(s) -
Warren Matthew J.,
Roddam Louise F.,
Power Peter M.,
Terry Tamsin D.,
Jennings Michael P.
Publication year - 2004
Publication title -
fems immunology & medical microbiology
Language(s) - English
Resource type - Journals
eISSN - 1574-695X
pISSN - 0928-8244
DOI - 10.1016/j.femsim.2004.01.002
Subject(s) - neisseria meningitidis , pilin , biology , glycosylation , microbiology and biotechnology , neisseriaceae , neisseria , pilus , virology , genetics , bacteria , virulence , antibiotics , gene
Abstract Pilin is the major subunit of the essential virulence factor pili and is glycosylated at Ser63. In this study we investigated the gene pglI to determine whether it is involved in the biosynthesis of the pilin‐linked glycan of Neisseria meningitidis strain C311#3. A N. meningitidis C311#3 pglI mutant resulted in a change of apparent molecular weight in SDS–PAGE and altered binding of antisera, consistent with a role in the biosynthesis of the pilin‐linked glycan. These data, in conjunction with homology with well‐characterised acyltransferases suggests a specific role for pglI in the biosynthesis of the basal 2,4‐diacetamido‐2,4,6‐trideoxyhexose residue of the pilin‐linked glycan.